ID A0A163KQN5_DIDRA Unreviewed; 854 AA.
AC A0A163KQN5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit C {ECO:0000256|HAMAP-Rule:MF_03002};
DE Short=eIF3c {ECO:0000256|HAMAP-Rule:MF_03002};
DE AltName: Full=Eukaryotic translation initiation factor 3 93 kDa subunit homolog {ECO:0000256|HAMAP-Rule:MF_03002};
DE Short=eIF3 p93 {ECO:0000256|HAMAP-Rule:MF_03002};
DE AltName: Full=Translation initiation factor eIF3, p93 subunit homolog {ECO:0000256|HAMAP-Rule:MF_03002};
GN Name=NIP1 {ECO:0000256|HAMAP-Rule:MF_03002,
GN ECO:0000313|EMBL:KZM27174.1};
GN ORFNames=EKO05_0004671 {ECO:0000313|EMBL:UPX14181.1}, EKO05_003896
GN {ECO:0000313|EMBL:KAF9708957.1}, ST47_g1697
GN {ECO:0000313|EMBL:KZM27174.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM27174.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM27174.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM27174.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
RN [2] {ECO:0000313|EMBL:KAF9708957.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9708957.1};
RA Syme R.A., Farfan-Caceres L., Lichtenzveig J.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF9708957.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9708957.1};
RX PubMed=32345704; DOI=10.1534/g3.120.401265;
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RT "Reference Genome Assembly for Australian Ascochyta rabiei Isolate
RT ArME14.";
RL G3 (Bethesda) 10:2131-2140(2020).
RN [4] {ECO:0000313|EMBL:KAF9708957.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9708957.1};
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:UPX14181.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:UPX14181.1};
RA Mobegi F.M., Debler J.W.D., Lee R.C.L.;
RL Submitted (MAR-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is involved in protein synthesis of a
CC specialized repertoire of mRNAs and, together with other initiation
CC factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC ribosome. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation.
CC {ECO:0000256|HAMAP-Rule:MF_03002}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03002}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000256|HAMAP-
CC Rule:MF_03002}.
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DR EMBL; RYYQ01000007; KAF9708957.1; -; Genomic_DNA.
DR EMBL; JYNV01000077; KZM27174.1; -; Genomic_DNA.
DR EMBL; CP095294; UPX14181.1; -; Genomic_DNA.
DR STRING; 5454.A0A163KQN5; -.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR Proteomes; UP000617380; Chromosome 7.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR HAMAP; MF_03002; eIF3c; 1.
DR InterPro; IPR027516; EIF3C.
DR InterPro; IPR008905; EIF3C_N_dom.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13937; EUKARYOTIC TRANSLATION INITATION FACTOR 3, SUBUNIT 8 EIF3S8 -RELATED; 1.
DR PANTHER; PTHR13937:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT C-RELATED; 1.
DR Pfam; PF05470; eIF-3c_N; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03002};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_03002};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03002}; Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT DOMAIN 599..773
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..202
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 12..44
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 96540 MW; 7C6A5D753371E126 CRC64;
MSRFFAASDS SSDESSEEEL YSNDEASEQE DSEVDSDDDS GDSDSSSGSE TGANRFLKDV
SSDSESDNED DTKPLKSAKD KRFDELEAVV RQIENAQRIN DWAVISDHFD KLNRLVPTLI
KQNDGKVPKM YIQTIADLET TVLETHEKQK VTPKKMNAIN QRGFNAIRQK VKKHNRDYQR
DIDSYRENKE EFMKEVEVVE QAPKEKKKKD KSRIAQLGTE TVIDAGDDGF VTVGAGGKAV
QYTAEGILKQ LRSIVEQRGR KNTDKLEQIR TMEKLFDVAV NDYQRIRVLL TLISTRFDLT
SGTASHMHQE QWKLADQEFG KLLQILENSN EIVVVENAEE WEDDEKTPTI EDGQIFKIPG
SVVSFVERLD DELTRSLQHI DPHTAEYVER LRDESALYAQ LVRASIYVDS LQKREGIEVP
QESANRVVIR RLEHVYFKPS AVVQILETKT WESIPSTLDS DTTPRSLSND TSSLVQTLCT
YLFKHSEGII RARAMLCQIY FLALHDQYYK ARDMMLMSHL QETISNFDVN TQILFNRSLV
QVGLCAFRAG LVYEAQTSLQ EICGSNRQKE LLAQGLQMQR YSQISPEQER LERQRQLPFH
LHINLELLEC VYLTCSMLLE IPLLAQLGSS PDLRKRVISK TYRRLLEYHE RQIFTGPPEN
TRDHVMQASK ALSAGEWKKA AEFINSIKIW ELTANAEQIK DMLSAQIQEE GLRTYLFTYA
PYYDTLAIST LADMFELSER KISAIVSKMI SHEELGAALD QVNSAVIFRK GVELSRLQTL
ALSLSDKASG LIESNEKTLE QRTQGTAHAF ERQGGRGGRG GGRGGRGGRG GGGGPRGGRN
QQFTGGALGR AIQA
//
